VGLU2_MOUSE
ID VGLU2_MOUSE Reviewed; 582 AA.
AC Q8BLE7; Q920B7;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 132.
DE RecName: Full=Vesicular glutamate transporter 2 {ECO:0000250|UniProtKB:Q9P2U8};
DE Short=VGluT2 {ECO:0000303|PubMed:16942593};
DE AltName: Full=Differentiation-associated BNPI {ECO:0000250|UniProtKB:Q9P2U8};
DE AltName: Full=Differentiation-associated Na(+)-dependent inorganic phosphate cotransporter {ECO:0000250|UniProtKB:Q9P2U8};
DE AltName: Full=Solute carrier family 17 member 6;
GN Name=Slc17a6 {ECO:0000312|MGI:MGI:2156052}; Synonyms=Dnpi, Vglut2;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TRANSPORTER ACTIVITY, ACTIVITY
RP REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, AND TISSUE SPECIFICITY.
RX PubMed=11432869; DOI=10.1074/jbc.m104578200;
RA Bai L., Xu H., Collins J.F., Ghishan F.K.;
RT "Molecular and functional analysis of a novel neuronal vesicular glutamate
RT transporter.";
RL J. Biol. Chem. 276:36764-36769(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Corpora quadrigemina;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Eye;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP DEVELOPMENTAL STAGE.
RX PubMed=12384506; DOI=10.1074/jbc.m206738200;
RA Schaefer M.K.-H., Varoqui H., Defamie N., Weihe E., Erickson J.D.;
RT "Molecular cloning and functional identification of mouse vesicular
RT glutamate transporter 3 and its expression in subsets of novel excitatory
RT neurons.";
RL J. Biol. Chem. 277:50734-50748(2002).
RN [5]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=15103023; DOI=10.1073/pnas.0401764101;
RA Wojcik S.M., Rhee J.S., Herzog E., Sigler A., Jahn R., Takamori S.,
RA Brose N., Rosenmund C.;
RT "An essential role for vesicular glutamate transporter 1 (VGLUT1) in
RT postnatal development and control of quantal size.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7158-7163(2004).
RN [6]
RP TISSUE SPECIFICITY, AND DEVELOPMENTAL STAGE.
RX PubMed=15118123; DOI=10.1126/science.1097468;
RA Fremeau R.T. Jr., Kam K., Qureshi T., Johnson J., Copenhagen D.R.,
RA Storm-Mathisen J., Chaudhry F.A., Nicoll R.A., Edwards R.H.;
RT "Vesicular glutamate transporters 1 and 2 target to functionally distinct
RT synaptic release sites.";
RL Science 304:1815-1819(2004).
RN [7]
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=16942593; DOI=10.1111/j.1471-4159.2006.04144.x;
RA Herzog E., Takamori S., Jahn R., Brose N., Wojcik S.M.;
RT "Synaptic and vesicular co-localization of the glutamate transporters
RT VGLUT1 and VGLUT2 in the mouse hippocampus.";
RL J. Neurochem. 99:1011-1018(2006).
RN [8]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17108179; DOI=10.1523/jneurosci.2556-06.2006;
RA Moechars D., Weston M.C., Leo S., Callaerts-Vegh Z., Goris I., Daneels G.,
RA Buist A., Cik M., van der Spek P., Kass S., Meert T., D'Hooge R.,
RA Rosenmund C., Hampson R.M.;
RT "Vesicular glutamate transporter VGLUT2 expression levels control quantal
RT size and neuropathic pain.";
RL J. Neurosci. 26:12055-12066(2006).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [10]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=25433636; DOI=10.1016/j.neuron.2014.11.008;
RA Preobraschenski J., Zander J.F., Suzuki T., Ahnert-Hilger G., Jahn R.;
RT "Vesicular glutamate transporters use flexible anion and cation binding
RT sites for efficient accumulation of neurotransmitter.";
RL Neuron 84:1287-1301(2014).
RN [11]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=30936473; DOI=10.1038/s41556-019-0301-x;
RA Nguyen M.T., Vemaraju S., Nayak G., Odaka Y., Buhr E.D., Alonzo N.,
RA Tran U., Batie M., Upton B.A., Darvas M., Kozmik Z., Rao S., Hegde R.S.,
RA Iuvone P.M., Van Gelder R.N., Lang R.A.;
RT "An opsin 5-dopamine pathway mediates light-dependent vascular development
RT in the eye.";
RL Nat. Cell Biol. 21:420-429(2019).
RN [12]
RP FUNCTION, AND TRANSPORTER ACTIVITY.
RX PubMed=33440152; DOI=10.1016/j.celrep.2020.108623;
RA Cheret C., Ganzella M., Preobraschenski J., Jahn R., Ahnert-Hilger G.;
RT "Vesicular Glutamate Transporters (SLCA17 A6, 7, 8) Control Synaptic
RT Phosphate Levels.";
RL Cell Rep. 34:108623-108623(2021).
CC -!- FUNCTION: Multifunctional transporter that transports L-glutamate as
CC well as multiple ions such as chloride, proton, potassium, sodium and
CC phosphate (PubMed:17108179, PubMed:33440152, PubMed:25433636,
CC PubMed:11432869). At the synaptic vesicle membrane, mainly functions as
CC a uniporter which transports preferentially L-glutamate but also,
CC phosphate from the cytoplasm into synaptic vesicles at presynaptic
CC nerve terminals of excitatory neural cells (PubMed:17108179,
CC PubMed:11432869). The L-glutamate or phosphate uniporter activity is
CC electrogenic and is driven by the proton electrochemical gradient,
CC mainly by the electrical gradient established by the vacuolar H(+)-
CC ATPase across the synaptic vesicle membrane (PubMed:11432869). In
CC addition, functions as a chloride channel that allows a chloride
CC permeation through the synaptic vesicle membrane therefore affects the
CC proton electrochemical gradient and promotes synaptic vesicles
CC acidification (By similarity). Moreover, functions as a vesicular
CC K(+)/H(+) antiport allowing to maintain the electrical gradient and to
CC decrease chemical gradient and therefore sustain vesicular glutamate
CC uptake (PubMed:25433636). The vesicular H(+)/H(+) antiport activity is
CC electroneutral (PubMed:25433636). At the plasma membrane, following
CC exocytosis, functions as a symporter of Na(+) and phosphate from the
CC extracellular space to the cytoplasm allowing synaptic phosphate
CC homeostasis regulation (PubMed:33440152). The symporter activity is
CC driven by an inside negative membrane potential and is electrogenic
CC (PubMed:33440152). Also involved in the regulation of retinal hyaloid
CC vessel regression during postnatal development (PubMed:30936473). May
CC also play a role in the endocrine glutamatergic system of other tissues
CC such as pineal gland and pancreas (By similarity).
CC {ECO:0000250|UniProtKB:Q9JI12, ECO:0000269|PubMed:11432869,
CC ECO:0000269|PubMed:17108179, ECO:0000269|PubMed:25433636,
CC ECO:0000269|PubMed:30936473, ECO:0000269|PubMed:33440152}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-glutamate(out) = L-glutamate(in); Xref=Rhea:RHEA:66336,
CC ChEBI:CHEBI:29985; Evidence={ECO:0000269|PubMed:11432869};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H(+)(out) + K(+)(in) = H(+)(in) + K(+)(out);
CC Xref=Rhea:RHEA:29467, ChEBI:CHEBI:15378, ChEBI:CHEBI:29103;
CC Evidence={ECO:0000269|PubMed:25433636};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 Na(+)(out) + phosphate(out) = 3 Na(+)(in) + phosphate(in);
CC Xref=Rhea:RHEA:71255, ChEBI:CHEBI:29101, ChEBI:CHEBI:43474;
CC Evidence={ECO:0000269|PubMed:33440152};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=phosphate(in) = phosphate(out); Xref=Rhea:RHEA:32823,
CC ChEBI:CHEBI:43474; Evidence={ECO:0000250|UniProtKB:Q9JI12};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=chloride(in) = chloride(out); Xref=Rhea:RHEA:29823,
CC ChEBI:CHEBI:17996; Evidence={ECO:0000250|UniProtKB:Q9JI12};
CC -!- ACTIVITY REGULATION: Chloride channel activity is allosterically
CC activated by lumenal H(+) and Cl(-) leading to synaptic vesicles
CC acidification. The L-glutamate transport activity is allosterically
CC activated by lumenal H(+) and Cl(-). The allosteric requirement for
CC H(+) efficiently prevents non-vesicular efflux across the plasma
CC membrane (By similarity). The L-glutamate uniporter activity exhibits a
CC biphasic dependence on chloride concentration (PubMed:11432869).
CC {ECO:0000250|UniProtKB:Q9JI12, ECO:0000269|PubMed:11432869}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.2 mM for L-glutamate {ECO:0000269|PubMed:11432869};
CC KM=1.1 mM for L-glutamate {ECO:0000269|PubMed:11432869};
CC Vmax=1405 pmol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:11432869};
CC Vmax=1219 pmol/min/mg enzyme toward L-glutamate
CC {ECO:0000269|PubMed:11432869};
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:11432869};
CC -!- SUBCELLULAR LOCATION: Cytoplasmic vesicle, secretory vesicle, synaptic
CC vesicle membrane {ECO:0000269|PubMed:15103023,
CC ECO:0000269|PubMed:16942593}; Multi-pass membrane protein
CC {ECO:0000255}. Synapse, synaptosome {ECO:0000269|PubMed:16942593}. Cell
CC membrane {ECO:0000305|PubMed:33440152}; Multi-pass membrane protein
CC {ECO:0000255}.
CC -!- TISSUE SPECIFICITY: Expressed in brain. Expressed in hippocampal
CC neurons (at protein level). {ECO:0000269|PubMed:11432869,
CC ECO:0000269|PubMed:15103023, ECO:0000269|PubMed:15118123,
CC ECO:0000269|PubMed:16942593}.
CC -!- DEVELOPMENTAL STAGE: Expressed in brain throughout development.
CC Transiently expressed in hippocampal neurons during the first week
CC after birth, with expression decreasing thereafter.
CC {ECO:0000269|PubMed:12384506, ECO:0000269|PubMed:15118123}.
CC -!- DISRUPTION PHENOTYPE: Mice exhibit an elevated rate of perinatal
CC lethality (PubMed:17108179). Surviving animals display a strong
CC reduction in evoked glutamergic responses in thalamic neurons
CC (PubMed:17108179). Reduction of protein level in homozygous and
CC heterozygous knockouts leads to a graded reduction in the amplitude of
CC the postsynaptic response to single vesicle fusion in thalamic neurons,
CC consistent with a role for this protein in determining quantal size
CC (PubMed:17108179). Decrease in the number of retinal hyaloid vessels at
CC postnatal day 8 as a result of precocious regression (PubMed:30936473).
CC {ECO:0000269|PubMed:17108179, ECO:0000269|PubMed:30936473}.
CC -!- SIMILARITY: Belongs to the major facilitator superfamily. Sodium/anion
CC cotransporter family. VGLUT subfamily. {ECO:0000305}.
CC -!- CAUTION: The phosphorylation site Tyr-195 is located in a predicted
CC transmembrane region. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AF324864; AAL08941.1; -; mRNA.
DR EMBL; AK045409; BAC32349.1; -; mRNA.
DR EMBL; BC038375; AAH38375.1; -; mRNA.
DR CCDS; CCDS39969.1; -.
DR RefSeq; NP_543129.3; NM_080853.3.
DR AlphaFoldDB; Q8BLE7; -.
DR SMR; Q8BLE7; -.
DR BioGRID; 228333; 2.
DR IntAct; Q8BLE7; 2.
DR MINT; Q8BLE7; -.
DR STRING; 10090.ENSMUSP00000032710; -.
DR GlyGen; Q8BLE7; 3 sites.
DR iPTMnet; Q8BLE7; -.
DR PhosphoSitePlus; Q8BLE7; -.
DR SwissPalm; Q8BLE7; -.
DR MaxQB; Q8BLE7; -.
DR PaxDb; Q8BLE7; -.
DR PeptideAtlas; Q8BLE7; -.
DR PRIDE; Q8BLE7; -.
DR ProteomicsDB; 297882; -.
DR ABCD; Q8BLE7; 1 sequenced antibody.
DR DNASU; 140919; -.
DR GeneID; 140919; -.
DR KEGG; mmu:140919; -.
DR UCSC; uc009hcf.2; mouse.
DR CTD; 57084; -.
DR MGI; MGI:2156052; Slc17a6.
DR eggNOG; KOG2532; Eukaryota.
DR InParanoid; Q8BLE7; -.
DR OrthoDB; 497052at2759; -.
DR PhylomeDB; Q8BLE7; -.
DR TreeFam; TF313535; -.
DR Reactome; R-MMU-428643; Organic anion transporters.
DR SABIO-RK; Q8BLE7; -.
DR BioGRID-ORCS; 140919; 3 hits in 72 CRISPR screens.
DR ChiTaRS; Slc17a6; mouse.
DR PRO; PR:Q8BLE7; -.
DR Proteomes; UP000000589; Unplaced.
DR RNAct; Q8BLE7; protein.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0060076; C:excitatory synapse; ISO:MGI.
DR GO; GO:0016021; C:integral component of membrane; IBA:GO_Central.
DR GO; GO:0030285; C:integral component of synaptic vesicle membrane; ISO:MGI.
DR GO; GO:0043005; C:neuron projection; ISS:UniProtKB.
DR GO; GO:1990030; C:pericellular basket; ISO:MGI.
DR GO; GO:0098793; C:presynapse; IDA:MGI.
DR GO; GO:0008021; C:synaptic vesicle; IDA:MGI.
DR GO; GO:0030672; C:synaptic vesicle membrane; ISS:UniProtKB.
DR GO; GO:0005254; F:chloride channel activity; ISS:UniProtKB.
DR GO; GO:0005313; F:L-glutamate transmembrane transporter activity; IDA:MGI.
DR GO; GO:0022810; F:membrane potential driven uniporter activity; ISS:UniProtKB.
DR GO; GO:0005326; F:neurotransmitter transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0015386; F:potassium:proton antiporter activity; IDA:UniProtKB.
DR GO; GO:0005436; F:sodium:phosphate symporter activity; IDA:UniProtKB.
DR GO; GO:0022857; F:transmembrane transporter activity; IBA:GO_Central.
DR GO; GO:0006820; P:anion transport; IBA:GO_Central.
DR GO; GO:1990384; P:hyaloid vascular plexus regression; IMP:UniProtKB.
DR GO; GO:0051938; P:L-glutamate import; ISS:UniProtKB.
DR GO; GO:0015813; P:L-glutamate transmembrane transport; IMP:UniProtKB.
DR GO; GO:0098700; P:neurotransmitter loading into synaptic vesicle; ISO:MGI.
DR GO; GO:0001504; P:neurotransmitter uptake; IDA:MGI.
DR GO; GO:0055062; P:phosphate ion homeostasis; IDA:UniProtKB.
DR GO; GO:0050803; P:regulation of synapse structure or activity; IBA:GO_Central.
DR GO; GO:0044341; P:sodium-dependent phosphate transport; IDA:UniProtKB.
DR GO; GO:0035249; P:synaptic transmission, glutamatergic; IBA:GO_Central.
DR Gene3D; 1.20.1250.20; -; 2.
DR InterPro; IPR011701; MFS.
DR InterPro; IPR020846; MFS_dom.
DR InterPro; IPR036259; MFS_trans_sf.
DR Pfam; PF07690; MFS_1; 1.
DR SUPFAM; SSF103473; SSF103473; 1.
DR PROSITE; PS50850; MFS; 1.
PE 1: Evidence at protein level;
KW Antiport; Cell membrane; Chloride; Chloride channel; Cytoplasmic vesicle;
KW Glycoprotein; Ion channel; Ion transport; Membrane;
KW Neurotransmitter transport; Phosphate transport; Reference proteome;
KW Sodium; Sodium transport; Symport; Synapse; Synaptosome; Transmembrane;
KW Transmembrane helix; Transport.
FT CHAIN 1..582
FT /note="Vesicular glutamate transporter 2"
FT /id="PRO_0000318170"
FT TOPO_DOM 1..71
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 72..92
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 93..125
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 126..146
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 147..148
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 149..169
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 170..177
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 178..198
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 199..216
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 217..237
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 238..244
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 245..265
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 266..310
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 311..331
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 332..349
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 350..370
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 371..386
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 387..407
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 408..409
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 410..430
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 431..443
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT TRANSMEM 444..464
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 465..477
FT /note="Vesicular"
FT /evidence="ECO:0000255"
FT TRANSMEM 478..498
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 499..582
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT CARBOHYD 100
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 101
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 470
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
SQ SEQUENCE 582 AA; 64561 MW; 9F7A47C0E0C7A64D CRC64;
MESVKQRILA PGKEGIKNFA GKSLGQIYRV LEKKQDNRET IELTEDGKPL EVPEKKAPLC
DCTCFGLPRR YIIAIMSGLG FCISFGIRCN LGVAIVDMVN NSTIHRGGKV IKEKAKFNWD
PETVGMIHGS FFWGYIITQI PGGYIASRLA ANRVFGAAIL LTSTLNMLIP SAARVHYGCV
IFVRILQGLV EGVTYPACHG IWSKWAPPLE RSRLATTSFC GSYAGAVIAM PLAGILVQYT
GWSSVFYVYG SFGMVWYMFW LLVSYESPAK HPTITDEERR YIEESIGESA NLLGAMEKFK
TPWRKFFTSM PVYAIIVANF CRSWTFYLLL ISQPAYFEEV FGFEISKVGM LSAVPHLVMT
IIVPIGGQIA DFLRSKQILS TTTVRKIMNC GGFGMEATLL LVVGYSHTRG VAISFLVLAV
GFSGFAISGF NVNHLDIAPR YASILMGISD GVGTLSGMVC PIIVGAMTKN KSREEWQYVF
LIAALVHYGG VIFYALFASG EKQPWADPEE TSEEKCGFIH EDELDEETGD ITQNYINYGT
TKSYGATSQE NGGWPNGWEK KEEFVQEGAQ DAYTYKDRDD YS
